Conformational stability of Syrian hamster prion protein PrP(90-231)
Grabenauer, Megan, Wyttenbach, Thomas, Sanghera, Narinder, Slade, Susan E., Pinheiro, Teresa J. T., Scrivens, James H. and Bowers, Michael T.. (2010) Conformational stability of Syrian hamster prion protein PrP(90-231). Journal of the American Chemical Society, Vol.132 (No.26). pp. 8816-8818. ISSN 0002-7863Full text not available from this repository.
Official URL: http://dx.doi.org/10.1021/ja100243h
Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrPC) known as PrPSc. While PrPSc is known to be exceptionally stable and resistant to protease degradation, PrPC has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrPC consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Divisions:||Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)|
|Journal or Publication Title:||Journal of the American Chemical Society|
|Publisher:||American Chemical Society|
|Official Date:||7 July 2010|
|Number of Pages:||4|
|Page Range:||pp. 8816-8818|
|Access rights to Published version:||Restricted or Subscription Access|
|Funder:||Department for Environment, Food and Rural Affairs, U.K., National Institutes of Health|
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